Identification of the Crucial Residues in the Early Insertion of Pardaxin into Different Phospholipid Bilayers.
J Chem Inf Model
; 57(4): 929-941, 2017 04 24.
Article
en En
| MEDLINE
| ID: mdl-28301157
ABSTRACT
Antimicrobial peptides (AMPs) are part of the innate host defense system, and they are produced by living organisms to defend themselves against infections. Pardaxin is a cationic AMP with antimicrobial and antitumor activities that has potential to be used as a novel antibiotic or for drug delivery in cancer therapy. This peptide acts on the membrane of target cells and can lead to lysis using different mechanisms of action. Here, we conducted 4.5 µs all-atom molecular dynamics (MD) simulations to determine the critical fragments and residues of Pardaxin for early insertion into different lipid bilayers. Our results revealed that the N-terminal domain of the peptide, particularly the Phe 2 and (/or) Phe 3 residues, has a crucial role in early insertion, independent of the type of lipid bilayers.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fosfolípidos
/
Péptidos Catiónicos Antimicrobianos
/
Simulación de Dinámica Molecular
/
Venenos de los Peces
/
Membrana Dobles de Lípidos
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
J Chem Inf Model
Asunto de la revista:
INFORMATICA MEDICA
/
QUIMICA
Año:
2017
Tipo del documento:
Article
País de afiliación:
Irán